FEBS Letters | |
The X‐ray crystal structure of β‐ketoacyl [acyl carrier protein] synthase I | |
Siggaard-Andersen, Mads2  Larsen, Sine1  Lindquist, Ylva1  Kadziola, Anders1  Olsen, Johan Gotthardt1  von Wettstein-Knowles, Penny2  | |
[1] Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark;Department of Genetics, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen, Denmark | |
关键词: Condensing enzyme; Protein structure; Fatty acid synthesis; Escherichia coli; KAS; β-ketoacyl [acyl carrier protein] synthase; FAS; fatty acid synthase; ACP; acyl carrier protein; NCS; non-crystallographic symmetry; PKS; polyketide synthase; | |
DOI : 10.1016/S0014-5793(99)01303-4 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The crystal structure of the fatty acid elongating enzyme β-ketoacyl [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been determined to 2.3 Å resolution by molecular replacement using the recently solved crystal structure of KAS II as a search model. The crystal contains two independent dimers in the asymmetric unit. KAS I assumes the thiolase αβαβα fold. Electrostatic potential distribution reveals an acyl carrier protein docking site and a presumed substrate binding pocket was detected extending the active site. Both subunits contribute to each substrate binding site in the dimer.
【 授权许可】
Unknown
【 预 览 】
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RO201912020308447ZK.pdf | 1225KB | download |